The anterior pituitary gonadotropins, Luteinizing Hormone (LH) and Follicle-Stimulating Hormone (FSH), have complex chemical structures because they are glycoproteins and because they are composed of a common alpha subunit as well as a hormone-specific beta subunit. Our laboratory has demonstrated that there is large molecular weight LH-like substance as well as heterologous subunit populations intracellularly and that a heterologous population of LH alpha subunits are released. It is likely that these molecular forms of the gonadotropins are related to their biosynthesis. In order to better understand the biosynthesis of these hormones, it is proposed to further define the molecular forms of LH and FSH involved in biosynthesis, to develop approaches to separate these molecular forms and to characterize them. Once this is accomplished, experiments will be performed to link these intermediates in sequence and time. The role of glycosylation in subunit combination will be investigated. A particular focal point of the proposed studies is to characterize the oligosaccharide moieties of chosen molecular forms with respect to size (number of carbohydrate residues per oligosaccharide), carbohydrate composition and carbohydrate structure. These studies should provide information regarding the role of the oligosaccharides, if any, in the biosynthesis of the pituitary gonadotropins.